YTA12_SCHPO
ID YTA12_SCHPO Reviewed; 773 AA.
AC Q9HGM3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mitochondrial respiratory chain complexes assembly protein rca1;
DE EC=3.4.24.-;
GN Name=yta12; ORFNames=SPBC543.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts as a component of the m-AAA protease complex which is a
CC ATP-dependent metalloprotease mediating degradation of non-assembled
CC mitochondrial inner membrane proteins. The complex is necessary for the
CC assembly of mitochondrial respiratory chain and ATPase complexes.
CC Function both in post-translational assembly and in the turnover of
CC mistranslated or misfolded polypeptides (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAC05251.1; -; Genomic_DNA.
DR RefSeq; NP_596797.1; NM_001023817.2.
DR AlphaFoldDB; Q9HGM3; -.
DR SMR; Q9HGM3; -.
DR BioGRID; 277594; 2.
DR STRING; 4896.SPBC543.09.1; -.
DR MEROPS; M41.A14; -.
DR SwissPalm; Q9HGM3; -.
DR MaxQB; Q9HGM3; -.
DR PaxDb; Q9HGM3; -.
DR PRIDE; Q9HGM3; -.
DR EnsemblFungi; SPBC543.09.1; SPBC543.09.1:pep; SPBC543.09.
DR GeneID; 2541079; -.
DR KEGG; spo:SPBC543.09; -.
DR PomBase; SPBC543.09; yta12.
DR VEuPathDB; FungiDB:SPBC543.09; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_16_2_1; -.
DR InParanoid; Q9HGM3; -.
DR OMA; YDKQGGG; -.
DR PhylomeDB; Q9HGM3; -.
DR PRO; PR:Q9HGM3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005745; C:m-AAA complex; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISS:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; ISO:PomBase.
DR Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..773
FT /note="Mitochondrial respiratory chain complexes assembly
FT protein rca1"
FT /id="PRO_0000317334"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 83..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 562
FT /evidence="ECO:0000250"
FT BINDING 336..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 638
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 773 AA; 85369 MW; E9263B76EAB9BEB9 CRC64;
MRNPFLTFRA PTRKTGDYLV SKFVKKDNFS SLRLARAYTF STRSTAVSQF SLLSLSQRSF
QSLKINKGIP EKHKIPLISS KQFSVTSKRS QNGSSGSNSD ANGRKNGQKN DDSKKKGLNG
NDPKKVFEIA LNGNTILGGI LVAYILYNVL SPNANMQEIT WQDFRQQFLD KGLVERLVVV
NRNMVRVILR GGVASGSGQY YFSIGSIDSF DRKLEDAQRQ LGIPPSEFVP VAYHDEVSVL
ATLLSFAPTL LIIGSVIYLS RRASGAAGGG QGGIFGIGKS RAKMFNHETD IKIKFADVAG
VDEAKEEIME FVKFLKNPKF YERLGAKIPR GAILSGPPGT GKTLLAKATA GEANVPFLSV
SGSEFLEMFV GVGPSRVRDL FATARKNAPC IIFIDEIDAI GKARGRGGQF GSNDERESTL
NQLLVEMDGF TSSEHIVVFA GTNRPDVLDP ALLRPGRFDR QITIDRPDIG GREQIFKVHL
KHIKAADNID LIAKRLAVLT SGFTGADIMN VCNEGALIAA RSNSNEVQMV HFEQAIERVT
AGLEKKSRVL SPEEKNTVAH HEAGHAVAGW FMEYVDPLLK VSIIPRAQAL GYASYLPKDQ
YLMSRGQILD QMGMALAGRV SEEIFFGPEK ITSGASDDFQ KVTRMAQAYV TQYGMSPTVG
TIAYPIDTRE TVQKPFSEAT AQMIDEEIRK LVKHAYERTK KLLLEHKQGL ENIAQRLLQK
EVITYNEVET ILGPRPYAYK HLNISELMRQ SEYKNDHDPR NPPIPPSPQQ PSA
